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Literature summary extracted from

  • Zhang, T.; Zhang, R.; Xu, M.; Zhang, X.; Yang, T.; Liu, F.; Yang, S.; Rao, Z.
    Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production (2018), Process Biochem., 70, 117-123 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.11 gene panD, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein Bacillus subtilis
4.1.1.11 gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein Corynebacterium glutamicum
4.1.1.11 gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein Lactiplantibacillus plantarum

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.11 D41G site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type Bacillus subtilis
4.1.1.11 E56S site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel Bacillus subtilis
4.1.1.11 K63E site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.11 L-aspartate Corynebacterium glutamicum
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Escherichia coli
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Bacillus subtilis
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Lactiplantibacillus plantarum
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Bacillus subtilis 168
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1
-
 beta-alanine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.11 Bacillus subtilis P52999
-
-
4.1.1.11 Bacillus subtilis 168 P52999
-
-
4.1.1.11 Corynebacterium glutamicum Q9X4N0
-
-
4.1.1.11 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 Q9X4N0
-
-
4.1.1.11 Escherichia coli P0A790
-
-
4.1.1.11 Lactiplantibacillus plantarum Q88Z02
-
-
4.1.1.11 Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 Q88Z02
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.11 proteolytic modification bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site Corynebacterium glutamicum
4.1.1.11 proteolytic modification bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site Bacillus subtilis
4.1.1.11 proteolytic modification bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site Lactiplantibacillus plantarum
4.1.1.11 proteolytic modification bacterial ADC is usually translated into an inactive zymogen. The zymogen is proteolytically cleaved at the Gly24-Ser25 site. The Escherichia coli ADC requires a Gcn5-like N-acetyltransferase, named PanM (also called PanZ), to help it reach complete maturation Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.11 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bacillus subtilis
4.1.1.11 recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Corynebacterium glutamicum
4.1.1.11 recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Lactiplantibacillus plantarum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.11 1.5
-
 pH 7.0, 37°C, recombinant enzyme Lactiplantibacillus plantarum
4.1.1.11 2.4
-
 pH 7.0, 37°C, recombinant enzyme Corynebacterium glutamicum
4.1.1.11 4.7
-
 pH 7.0, 37°C, recombinant enzyme Bacillus subtilis
4.1.1.11 5.5
-
 pH 7.0, 70°C, recombinant enzyme Lactiplantibacillus plantarum
4.1.1.11 9.6
-
 pH 7.0, 70°C, recombinant enzyme Corynebacterium glutamicum
4.1.1.11 15.7
-
 pH 7.0, 65°C, recombinant enzyme Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.11 L-aspartate
-
 Corynebacterium glutamicum beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Escherichia coli beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Bacillus subtilis beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Lactiplantibacillus plantarum beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Bacillus subtilis 168 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 beta-alanine + CO2
-
 ?
4.1.1.11 L-aspartate
-
 Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 beta-alanine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.11 tetramer the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit Corynebacterium glutamicum
4.1.1.11 tetramer the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit Escherichia coli
4.1.1.11 tetramer the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit Bacillus subtilis
4.1.1.11 tetramer the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit Lactiplantibacillus plantarum

Synonyms

EC Number Synonyms Comment Organism
4.1.1.11 ADC
-
 Corynebacterium glutamicum
4.1.1.11 ADC
-
 Escherichia coli
4.1.1.11 ADC
-
 Bacillus subtilis
4.1.1.11 ADC
-
 Lactiplantibacillus plantarum
4.1.1.11 BsADC
-
 Bacillus subtilis
4.1.1.11 BsADC
-
 Lactiplantibacillus plantarum
4.1.1.11 CgADC
-
 Corynebacterium glutamicum
4.1.1.11 GcADC
-
 Escherichia coli
4.1.1.11 L-Aspartate alpha-decarboxylase
-
 Corynebacterium glutamicum
4.1.1.11 L-Aspartate alpha-decarboxylase
-
 Escherichia coli
4.1.1.11 L-Aspartate alpha-decarboxylase
-
 Bacillus subtilis
4.1.1.11 L-Aspartate alpha-decarboxylase
-
 Lactiplantibacillus plantarum
4.1.1.11 PanD
-
 Corynebacterium glutamicum
4.1.1.11 PanD
-
 Escherichia coli
4.1.1.11 PanD
-
 Bacillus subtilis
4.1.1.11 PanD
-
 Lactiplantibacillus plantarum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.11 65
-
 recombinant enzyme Bacillus subtilis
4.1.1.11 70
-
 recombinant enzyme Corynebacterium glutamicum
4.1.1.11 70
-
 recombinant enzyme Lactiplantibacillus plantarum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.1.1.11 35 90 measured range, activity profile overview Corynebacterium glutamicum
4.1.1.11 35 90 measured range, activity profile overview Bacillus subtilis
4.1.1.11 35 90 measured range, activity profile overview Lactiplantibacillus plantarum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.11 6.5
-
 recombinant enzyme Corynebacterium glutamicum
4.1.1.11 6.5
-
 recombinant enzyme Lactiplantibacillus plantarum
4.1.1.11 7
-
 recombinant enzyme Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.11 4 11 activity range, profile overview Corynebacterium glutamicum
4.1.1.11 4 11 activity range, profile overview Lactiplantibacillus plantarum
4.1.1.11 5 10 activity range, profile overview Bacillus subtilis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.1.1.11 Bacillus subtilis enzyme mutant K63E, sequence calculation
-
 5.12
4.1.1.11 Bacillus subtilis wild-type enzyme, sequence calculation
-
 5.6
4.1.1.11 Bacillus subtilis enzyme mutant D41G, sequence calculation
-
 5.65
4.1.1.11 Bacillus subtilis enzyme mutant E56S, sequence calculation
-
 6.09

General Information

EC Number General Information Comment Organism
4.1.1.11 evolution there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor Corynebacterium glutamicum
4.1.1.11 evolution there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor Escherichia coli
4.1.1.11 evolution there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor Bacillus subtilis
4.1.1.11 evolution there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor Lactiplantibacillus plantarum
4.1.1.11 malfunction the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production. The E56S mutant shows an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuated the mechanism-based inactivation of the enzyme Bacillus subtilis
4.1.1.11 additional information structural homology modeling BsADC using the Escherichia coli ADC structure, PDB ID 1PQE, as template Bacillus subtilis
4.1.1.11 physiological function L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid Corynebacterium glutamicum
4.1.1.11 physiological function L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid Escherichia coli
4.1.1.11 physiological function L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid Bacillus subtilis
4.1.1.11 physiological function L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid Lactiplantibacillus plantarum